Lysyl oxidase: Properties, specificity, and biological roles inside and outside of the cell
Lysyl oxidase: Properties, specificity, and biological roles inside and outside of the cell
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DOI：
10.1002/jcb.10413
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发表时间：
2003-03-01
影响因子：
4
通讯作者：
Li, WD
中科院分区：
文献类型：
--
作者：
Kagan, HM;Li, WD
赖氨酰氧化酶（L0）通过氧化弹性蛋白和胶原中的赖氨酸残基，从而引发稳定这些纤维蛋白的共价交联的形成，在细胞外基质（ECM）的形成和修复中起关键作用。它的催化活性取决于它的铜辅因子和一个独特的羰基辅因子，并已被证明延伸到各种碱性球状蛋白，包括组蛋白H1。虽然LO的三维结构尚未确定，本论文提供了基于其主要序列的假设，这可能是其不寻常的底物特异性的突出的静电成分，以及催化抑制功能的propeptide结构域的脯氨酰氧化酶。最近的研究表明，LO似乎在细胞内的方式，这强烈修改细胞活性的功能。新发现的LO样蛋白也可能在生物学中发挥独特的作用。
Lysyl oxidase (LO) plays a critical role in the formation and repair of the extracellular matrix (ECM) by oxidizing lysine residues in elastin and collagen, thereby initiating the formation of covalent crosslinkages which stabilize these fibrous proteins. Its catalytic activity depends upon both its copper cofactor and a unique carbonyl cofactor and has been shown to extend to a variety of basic globular proteins, including histone H1. Although the three-dimensional structure of LO has yet to be determined, the present treatise offers hypotheses based upon its primary sequence, which may underlie the prominent electrostatic component of its unusual substrate specificity as well as the catalysis-suppressing function of the propeptide domain of prolysyl oxidase. Recent studies have demonstrated that LO appears to function within the cell in a manner, which strongly modifies cellular activity. Newly discovered LO-like proteins also likely play unique roles in biology.